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  • 1
    Electronic Resource
    Electronic Resource
    The Role of Posttranscriptional Modification in Stabilization of Transfer RNA from Hyperthermophiles (1994)
    s.l. : American Chemical Society
    Biochemistry 33 (1994), S. 7869-7876 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00191a014
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  • 2
    Electronic Resource
    Electronic Resource
    Structure of a molecular chaperone from a thermophilic archaebacterium (1993)
    [s.l.] : Nature Publishing Group
    Nature 361 (1993), S. 475-477 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] When negatively stained and examined by transmission electron microscopy, the thermosome adopts two distinct orientations with respect to the carbon film to give characteristic end and side views1 (Fig. la, c, d). End views comprise a ring with eightfold radial (pseudo)symmetry enclosing a central ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/361475a0
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  • 3
    Electronic Resource
    Electronic Resource
    DNA topoisomerase V is a relative of eukaryotic topoisomerase I from a hyperthermophilic prokaryote (1993)
    [s.l.] : Nature Publishing Group
    Nature 364 (1993), S. 735-737 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Topoisomerase V was isolated and purified almost to homogeneity from M. kandleri using its ability to relax positively and negatively supercoiled DNA without magnesium (Fig. 1). According to the gel-filtration calibration standards, the peak of activity migrates as a globular protein with Mr ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/364735a0
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  • 4
    Electronic Resource
    Electronic Resource
    Two N 5, N 10-methylenetetrahydromethanopterin dehydrogenases in the extreme thermophile Methanopyrus kandleri: characterization of the coenzyme F420-dependent enzyme (1993)
    Springer
    Archives of microbiology 160 (1993), S. 186-192 
    Details
    ISSN: 1432-072X
    Keywords: Coenzyme F420 ; Tetrahydromethanopterin ; Hydrogenase ; H2-forming methylenetrahydromethanopterin dehydrogenase ; Methanobacterium thermoautotrophicum ; Methanosarcina barkeri ; Archaeoglobus fulgidus
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract It was recently reported that the extreme thermophile Methanopyrus kandleri contains only a H2-forming N 5, N 10-methylenetetrahydromethanopterin dehydrogenase which uses protons as electron acceptor. We describe here the presence in this Archaeon of a second N 5,N 10-methylenetetrahydromethanopterin dehydrogenase which is coenzyme F420-dependent. This enzyme was purified and characterized. The enzyme was colourless, had an apparent molecular mass of 300 kDa, an isoelectric point of 3.7±0.2 and was composed of only one type of subunit of apparent molecular mass of 36 kDa. The enzyme activity increased to an optimum with increasing salt concentrations. Optimal salt concentrations were e.g. 2 M (NH4)2SO4, 2 M Na2HPO4, 1.5 M K2HPO4, and 2 M NaCl. In the absence of salts the enzyme exhibited almost no activity. The salts affected mainly the V max rather than the K m of the enzyme. The catalytic mechanism of the dehydrogenase was determined to be of the ternary complex type, in agreement with the finding that the enzyme lacked a chromophoric prosthetic group. In the presence of M (NH4)2SO4 the V max was 4000 U/mg (k cat=2400 s-1) and the K m for N 5,N 10-methylenetetrahydromethanopterin and for coenzyme F420 were 80 μM and 20 μM, respectively. The enzyme was relatively heat-stable and lost no activity when incubated anaerobically in 50 mM K2HPO4 at 90°C for one hour. The N-terminal amino acid sequence was found to be similar to that of the F420-dependent N 5, N 10-methylenetetrahydromethanopterin dehydrogenase from Methanobacterium thermoautotrophicum, Methanosarcina barkeri, and Archaeoglobus fulgidus.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00249123
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  • 5
    Electronic Resource
    Electronic Resource
    Flexistipes sinusarabici, a novel genus and species of eubacteria occurring in the Atlantis II Deep brines of the Red Sea (1990)
    Springer
    Archives of microbiology 154 (1990), S. 120-126 
    Details
    ISSN: 1432-072X
    Keywords: Flexistipes ; Eubacteria ; Atlantis II Deep brines ; Red Sea
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Four isolates of a gram-negative flexible bacterium have been obtained from brine water samples of the Atlantis II Deep of the Red Sea at a depth of 2000 m. One isolate (MAS 10) was studied in detail. Cells are nonmotile, flexible rods, measuring about 0.3 μm in width and 5 to 50 μm in length. The new organisms are heterotrophs growing anaerobically on yeast extract, meat extract, peptone, tryptone, and, less efficiently, on acetate and casamino acids. Growth occurs between 30% and 53°C at pH 6 to 8 in the presence of at least 3% NaCl. The shortest doubling time is 8.5 h under optimal growth conditions. Cells are sensitive to the antibiotics penicillin, ampicillin, vancomycin, and streptomycin, but resistant to tetracyclin and rifamipicin. The GC-content of the DNA is 39 mol%. Based on their 16S rRNA the new isolates group with the general cluster of eubacterial phyla. Since they show no specific relationship to any of them, a new genus is described, which is named Flexistipes, the flexible stick. Type species is Flexistipes sinusarabici strain MAS 10 (DSM 4947).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00423320
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  • 6
    Electronic Resource
    Electronic Resource
    Thermococcus litoralis sp. nov.: A new species of extremely thermophilic marine archaebacteria (1990)
    Springer
    Archives of microbiology 153 (1990), S. 205-207 
    Details
    ISSN: 1432-072X
    Keywords: Archaebacteria ; Extreme thermophile ; Pyrococcus ; Thermococcus
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We describe a new species, Thermococcus litoralis, which is different from the type species Thermococcus celer in molecular, morphological and physiological characteristics.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00247822
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  • 7
    Electronic Resource
    Electronic Resource
    Fervidobacterium islandicum sp. nov., a new extremely thermophilic eubacterium belonging to the “Thermotogales” (1990)
    Springer
    Archives of microbiology 154 (1990), S. 105-111 
    Details
    ISSN: 1432-072X
    Keywords: Eubacterium ; Thermophile ; Evolution ; Fervidobacterium ; Lipids ; Thermotoga
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract An extremely thermophilic anaerobic fermentative eubacterium growing at temperatures between 50 and 80°C (opt.: 65°C) was isolated from an Icelandic hot spring. The cells were Gram-negative motile rods, about 1.8 μm in length, and 0.6 μm in width occurring singly and in pairs. About 50% of the cells formed large spheroids at one end similar to Fervidobacterium nodosum. The new isolate H 21 differed from Fervidobacterium nodosum by a 6 mol % higher GC-content of its DNA (41 mol %), its ability to grow on cellulose, and insignificant DNA homology. The lipids of isolate H 21 were similar to that of members of “Thermotogales”. 16S rRNA sequencing of isolate H 21 and Fervidobacterium nodosum indicated (a) that isolate H 21 represents a new species of the genus Fervidobacterium which we name Fervidobacterium islandicum and (b) that the genus Fervidobacterium belongs to the “Thermotogales” branch.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00423318
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  • 8
    Electronic Resource
    Electronic Resource
    Methanopyrus kandleri, gen. and sp. nov. represents a novel group of hyperthermophilic methanogens, growing at 110°C (1991)
    Springer
    Archives of microbiology 156 (1991), S. 239-247 
    Details
    ISSN: 1432-072X
    Keywords: Methanopyrus ; Methanogens ; Archaea ; Hyperthermophilic ; Marine ; Vents
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A novel group of hyperthermophilic rod-shaped motile methanogens was isolated from a hydrothermally heated deep sea sediment (Guaymas Basin, Gulf of California) and from a shallow marine hydrothermal system (Kolbeinsey ridge, Iceland). The grew between 84 and 110°C (opt: 98°C) and from 0.2% to 4% NaCl (opt. 2%) and pH 5.5 to 7 (opt: 6.5). The isolates were obligate chemolithoautotrophes using H2/CO2 as energy and carbon sources. In the presence of sulfur, H2S was formed and cells tended to lyse. The cell wall consisted of a new type of pseudomurein containing ornithin in addition to lysine and no N-acetylglucosamine. The pseudomurein layer was covered by a detergent-sensitive protein surface layer. The core lipid consisted exclusively of phytanyl diether. The GC content of the DNA was 60 mol%. By 16S rRNA comparisons the new organisms were not related to any of the three methanogenic lineages. Based on the physiological and molecular properties of the new isolates, we describe here a new genus, which we name Methanopyrus (the “methane fire”). The type species is Methanopyrus kandleri (type strain: AV19; DSM 6324).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00262992
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  • 9
    Electronic Resource
    Electronic Resource
    Thiobacillus plumbophilus spec. nov., a novel galena and hydrogen oxidizer (1992)
    Springer
    Archives of microbiology 157 (1992), S. 213-217 
    Details
    ISSN: 1432-072X
    Keywords: Thiobacillus ; Galena ; Hydrogen oxidation ; Chemolithotrophic
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract From an uranium mine three strains of rodshaped, mesophilic, chemolithoautotrophic bacteria were isolated. They grow by oxidation of H2S, galena (PbS) and H2. Anglesite (PbSO4) is formed from galena. No ferrous iron is oxidized by the isolates. They grow between pH 4 and 6.5 at temperatures of about 9 to 41°C (optimum around 27°C). The G+C content of the DNA is around 66 mol %. Based on their ability to oxidize sulfur compounds, the new organisms belong to the genus Thiobacillus. No significant homology with Thiobacillus ferrooxidans and Thiobacillus cuprinus was detected by DNA-DNA hybridization. Therefore the new isolates represent a new species within the genus Thiobacillus. Based on the unusual growth on galena, we name the new species Thiobacillus plumbophilus (type strain Gro 7; DSM 6690).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00245152
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  • 10
    Electronic Resource
    Electronic Resource
    A F420-dependent NADP reductase in the extremely thermophilic sulfate-reducing Archaeoglobus fulgidus (1993)
    Springer
    Archives of microbiology 160 (1993), S. 199-205 
    Details
    ISSN: 1432-072X
    Keywords: Archaea ; Sulfate reducers ; Hyperthermophiles ; Coenzyme F420 ; Deazaflavin ; F420-dependent NADP reducatase ; Stereoselectivity ; Stereospecificity ; Archaeoglobus fulgidus
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Archaeoglobus fulgidus, a sulfate-reducing Archaeon with a growth temperature optimum of 83°C, uses the 5-deazaflavin coenzyme F420 rather than pyridine nucleotides in catabolic redox processes. The organism does, however, require reduced pyridine nuclcotides for biosynthetic purposes. We describe here that the Archaeon contains a coenzyme F420-dependent NADP reductase which links anabolism to catabolism. The highly thermostable enzyme was purfied 3600-fold by affinity chromatography to apparent homogeneity in a 60% yield. The native enzyme with an apparent molecular mass of 55 kDa was composed of only one type of subunit of apparent molecular mass of 28 kDa. Spectroscopic analysis of the enzyme did not reveal the presence of any chromophoric prosthetic group. The purified enzyme catalyzed the reversible reduction of NADP (apparent K M 40 μM) with reduced F420 (apparent K M 20μM) with a specific activity of 660 U/mg (apparent V max) at pH 8.0 (pH optimum) and 80°C (temperature optimum). It was specific for both coenzyme F420 and NADP. Sterochemical investigations showed that the F420-dependent NADP reductase was Si face specific with respect to C5 of F420 and Si face specific with respect to C4 of NADP.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00249125
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